Difference between revisions of "PsdR"

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'''Additional publications:''' {{PubMed|21283517}}
 
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<pubmed>10094672,18394148,14651641</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:49, 30 May 2012

  • Description: two-component response regulator, induction of psdA-psdB in response to lipid II-binding lantibiotics, such as nisin and gallidermin

Gene name psdR
Synonyms yvcP
Essential no
Product two-component response regulator
Function resistance against toxic peptides
Interactions involving this protein in SubtInteract: PsdR
MW, pI 27 kDa, 4.676
Gene length, protein length 711 bp, 237 aa
Immediate neighbours psdS, yvcN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YvcP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PsdR expression.png
























Categories containing this gene/protein

transcription factors and their control, resistance against toxins/ antibiotics, phosphoproteins

This gene is a member of the following regulons

The PsdR regulon: psdA-psdB

The gene

Basic information

  • Locus tag: BSU34720

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: OmpR family of two-component response regulators
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated by PsdS on an Asp residue
  • Cofactor(s):
  • Effectors of protein activity: phosphorylation likely affects DNA-binding activity

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Stéphanie Coumes-Florens, Céline Brochier-Armanet, Annick Guiseppi, François Denizot, Maryline Foglino
A new highly conserved antibiotic sensing/resistance pathway in firmicutes involves an ABC transporter interplaying with a signal transduction system.
PLoS One: 2011, 6(1);e15951
[PubMed:21283517] [WorldCat.org] [DOI] (I e)

Anna Staroń, Dora Elisabeth Finkeisen, Thorsten Mascher
Peptide antibiotic sensing and detoxification modules of Bacillus subtilis.
Antimicrob Agents Chemother: 2011, 55(2);515-25
[PubMed:21078927] [WorldCat.org] [DOI] (I p)

Eva Rietkötter, Diana Hoyer, Thorsten Mascher
Bacitracin sensing in Bacillus subtilis.
Mol Microbiol: 2008, 68(3);768-85
[PubMed:18394148] [WorldCat.org] [DOI] (I p)

Thorsten Mascher, Neil G Margulis, Tao Wang, Rick W Ye, John D Helmann
Cell wall stress responses in Bacillus subtilis: the regulatory network of the bacitracin stimulon.
Mol Microbiol: 2003, 50(5);1591-604
[PubMed:14651641] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)